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Fast Magic‐Angle Spinning 19 F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies
Author(s) -
Wang Mingzhang,
Lu Manman,
Fritz Matthew P.,
Quinn Caitlin M.,
Byeon InJa L.,
Byeon ChangHyeock,
Struppe Jochem,
Maas Werner,
Gronenborn Angela M.,
Polenova Tatyana
Publication year - 2018
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201809060
Subject(s) - magic angle spinning , nuclear magnetic resonance spectroscopy , spectroscopy , solid state nuclear magnetic resonance , chemistry , chemical shift , indole test , capsid , magic angle , structural biology , spin diffusion , crystallography , fluorine 19 nmr , nuclear magnetic resonance , stereochemistry , diffusion , physics , biochemistry , quantum mechanics , gene , thermodynamics
19 F NMR spectroscopy is an attractive and growing area of research with broad applications in biochemistry, chemical biology, medicinal chemistry, and materials science. We have explored fast magic angle spinning (MAS) 19 F solid‐state NMR spectroscopy in assemblies of HIV‐1 capsid protein. Tryptophan residues with fluorine substitution at the 5‐position of the indole ring were used as the reporters. The 19 F chemical shifts for the five tryptophan residues are distinct, reflecting differences in their local environment. Spin‐diffusion and radio‐frequency‐driven‐recoupling experiments were performed at MAS frequencies of 35 kHz and 40–60 kHz, respectively. Fast MAS frequencies of 40–60 kHz are essential for consistently establishing 19 F– 19 F correlations, yielding interatomic distances of the order of 20 Å. Our results demonstrate the potential of fast MAS 19 F NMR spectroscopy for structural analysis in large biological assemblies.